STRING protein interaction network
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
azoRFmn dependent nadh:quinone oxidoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. The enzyme can reduce ethyl red and methyl red, but is not able to convert sulfonated azo dyes (201 aa)    
Predicted Functional Partners:
Nadph:quinone oxidoreductase mdab; NADPH-specific quinone reductase. Is most active with quinone derivatives and ferricyanide as electron acceptors. Can use menadione, 1,4-naphthoquinone and 1,4-benzoquinone
Putative nad(p)h-dependent oxidoreductase ycak; Belongs to the NAD(P)H dehydrogenase (quinone) family
Nitroreductase a, nadph-dependent, fmn-dependent; Catalyzes the reduction of nitroaromatic compounds using NADPH. Has a broad electron acceptor specificity. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major oxygen-insensitive nitroreductase in E.coli
Dihydropteridine reductase, nad(p)h-dependent, oxygen-insensitive; Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4- dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species
Chromate reductase, nad(p)h dehydrogenase (quinone); Catalyzes the reduction of quinones . Acts by simultaneous two-electron transfer, avoiding formation of highly reactive semiquinone intermediates and producing quinols that promote tolerance of H(2)O(2). Quinone reduction is probably the primary biological role of ChrR (By similarity). Can also reduce toxic chromate to insoluble and less toxic Cr(3+). Catalyzes the transfer of three electrons to Cr(6+) producing Cr(3+) and one electron to molecular oxygen without producing the toxic Cr(5+) species and only producing a minimal amount [...]
Potassium-efflux system ancillary protein for kefc, glutathione-regulated; Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC. Can use a wide range of substrates, including electrophilic quinones, and its function could be to reduce the redox toxicity of electrophilic quinones in parallel with acting as triggers for the KefC efflux system
Epoxyqueuosine reductase; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr)
Bicupin-related protein; Does not have quercetin 2,3-dioxygenase activity
N-methyltryptophan oxidase, fad-binding; Catalyzes the oxidative demethylation of N-methyl-L- tryptophan. Can also use other N-methyl amino acids, including sarcosine, which, however, is a poor substrate
Nad(p)h dehydrogenase (quinone); It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide. It prefers NADH over NADPH
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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